EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   2.7.11.2 | -999 |
- |
more |
binding of wild-type and mutant PDHK2 proteins to the unaltered L2 domain, kinetics |
672273 |
| 2.7.11.2 | -999 |
- |
more |
changes in ionic strength |
642145 |
| 2.7.11.2 | -999 |
- |
more |
dissociation constants for ADP and ATP binding, L2 binding increases affinities for both ADP and ATP |
661592 |
| 2.7.11.2 | -999 |
- |
more |
kinetics |
660805, 661094 |
| 2.7.11.2 | -999 |
- |
more |
kinetics and thermodynamics of PDK binding to L2 within the pyruvate dehydrogenase complex |
674640 |
| 2.7.11.2 | -999 |
- |
more |
pyruvate dehydrogenase complex components interaction dissociation constants and kinetics |
662151 |
| 2.7.11.2 | -999 |
- |
more |
the Km value for ADP depends on the presence and concentration of K+, effect of K+ on kinetic parameters |
642134 |
| 2.7.11.2 | 0.0006 |
- |
[pyruvate dehydrogenase (acetyl-transferring)] |
in presence of dihydrolipoyl transacetylase |
642133, 642136, 642137 |
| 2.7.11.2 | 0.0006 |
- |
[pyruvate dehydrogenase (acetyl-transferring)] |
pH 7.0, 30°C |
642136, 642137 |
| 2.7.11.2 | 0.0006 |
- |
[pyruvate dehydrogenase (acetyl-transferring)] |
pH 7.5, 30°C |
642133 |
